The use of extended amino acid motifs for focussing on toxic peptides in coeliac disease

Cullis, P, McLachlan, A and Cornell, H 2002, 'The use of extended amino acid motifs for focussing on toxic peptides in coeliac disease', Journal of Biochemistry, Molecular Biology and Biophysics, vol. 6, no. 5, pp. 319-324.


Document type: Journal Article
Collection: Journal Articles

Title The use of extended amino acid motifs for focussing on toxic peptides in coeliac disease
Author(s) Cullis, P
McLachlan, A
Cornell, H
Year 2002
Journal name Journal of Biochemistry, Molecular Biology and Biophysics
Volume number 6
Issue number 5
Start page 319
End page 324
Total pages 6
Publisher Taylor and Francis
Abstract Cereal prolamins of wheat, rye and barley are the major proteins that have been implicated in toxicity in patients with coeliac disease. The gliadins of wheat are the best characterised with the identification of toxic peptides from rye and barley not as well advanced. This study has employed extended motifs, based on the known toxic motifs are derived from the sequence of A-gliadin, to search protein databases for matches with coeliac-toxic cereals. The results obtained have provided pointers to specific regions in rye and barley prolamins, which have received little attention in in vitro and in vivo studies of toxicity in coeliac disease. The results obtained in this study indicate that the size of the extended motif is critical when searching for coeliac-toxic cereals using protein databases. Extended motifs that are common to all three coeliac-toxic cereals and found in active wheat gliadin peptides are QQPYP, PQQPY and QQQPFP.
Subject Medical Biochemistry: Proteins and Peptides (incl. Medical Proteomics)
DOI - identifier 10.1080/1025814021000003238
Copyright notice © McLachlan
ISSN 1025-8140
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